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Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complex.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2002 Jun 11; Vol. 99 (12), pp. 7962-7. - Publication Year :
- 2002
-
Abstract
- Phosducin and phosducin-like protein (PhLP) bind G protein betagamma subunits and regulate their activity. This report describes a previously uncharacterized binding partner unique to PhLP that was discovered by coimmunoprecipitation coupled with mass spectrometric identification. Chaperonin containing tailless complex polypeptide 1 (CCT), a cytosolic chaperone responsible for the folding of many cellular proteins, binds PhLP with a stoichiometry of one PhLP per CCT complex. Unlike protein-folding substrates of CCT, which interact only in their nonnative conformations, PhLP binds in its native state. Native PhLP competes directly for binding of protein substrates of CCT and thereby inhibits CCT activity. Overexpression of PhLP inhibited the ability of CCT to fold newly synthesized beta-actin by 80%. These results suggest that the interaction between PhLP and CCT may be a means to regulate CCT-dependent protein folding or alternatively, to control the availability of PhLP to modulate G protein signaling.
- Subjects :
- Actins metabolism
Animals
Binding, Competitive
CHO Cells
Carrier Proteins isolation & purification
Cloning, Molecular
Cricetinae
Cytosol metabolism
DNA, Complementary
Escherichia coli genetics
Kinetics
Mass Spectrometry
Molecular Chaperones
Nerve Tissue Proteins isolation & purification
Protein Folding
Rats
Recombinant Proteins isolation & purification
Recombinant Proteins metabolism
Transfection
Carrier Proteins metabolism
Chaperonins metabolism
Nerve Tissue Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0027-8424
- Volume :
- 99
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 12060742
- Full Text :
- https://doi.org/10.1073/pnas.112075699